Crystal structure of the EB1 C-terminal domain complexed with the CAP-Gly domain of p150Glued. Determined by X-ray diffraction at 1.8 Å resolution. Released 13 Sept 2005.
Explore 1TXQ in 3D Show helices and sheets RCSB PDB PDBe
1TXQ contains 3 α-helices and 8 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 32-35 | 4 | 1 |
| β-strand | 41-48 | 8 | 1 |
| β-strand | 57-62 | 6 | 1 |
| β-strand | 69 | 1 | 1 |
| β-strand | 72-73 | 2 | 2 |
| β-strand | 76-77 | 2 | 2 |
| β-strand | 86-89 | 4 | 1 |
| α-helix | 91-93 | 3 | |
| β-strand | 94-96 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 193-230 | 38 | |
| α-helix | 237-246 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dynactin 1 | A | protein | 93 | Homo sapiens | Q14203 (AlphaFold model) |
| Microtubule-associated protein RP/EB family member 1 | B | protein | 86 | Homo sapiens | Q15691 (AlphaFold model) |
>1TXQ_1 Dynactin 1 (chains A) GSRMSAEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQ GRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPE
>1TXQ_2 Microtubule-associated protein RP/EB family member 1 (chains B) NPGVGNGDDEAAELMQQVNVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRI VDILYATDEGFVIPDEGGPQEEQEEY
Structural Basis for the Activation of Microtubule Assembly by the EB1 and p150(Glued) Complex. Hayashi, I., Wilde, A., Mal, T.K. et al. Mol Cell (2005) 19:449-460. DOI 10.1016/j.molcel.2005.06.034 · PubMed
Other PDB entries of the same protein (UniProt Q14203 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1TXQ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.